Abstract
Phytochrome A is readily cleavable by proteolytic agents to yield an amino-terminal fragment of 66 kilodalton (kDa), which consists of residues 1 to approximately 600, and a dimer of the carboxy-terminal 55-kDa fragment, from residue 600 or so to the carboxyl terminus. The former domain, carrying the tetrapyrrole chromophore, has been studied extensively because of its photoactivity, while less attention has been paid to the non-chromophoric portion until quite recently. However, the evidence gathered to date suggests that this domain is also of great importance. We present here a review of the structure and the biochemical and physiological functions of the two domains, of parts of these domains, and of the cooperation between them.
Original language | English |
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Pages (from-to) | 109-122 |
Number of pages | 14 |
Journal | Journal of Plant Research |
Volume | 110 |
Issue number | 1 |
DOIs | |
Publication status | Published - Mar 1997 |
Externally published | Yes |
Keywords*
- Carboxy-terminal deletion (phytochrome)
- Domain structure (phytochrome)
- Photoconversion
- Phytochrome
- Structure and function (phytochrome)
- Transgenic plants
Field of Science*
- 1.6 Biological sciences
Publication Type*
- 1.1. Scientific article indexed in Web of Science and/or Scopus database